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Amanda Dynoske, Jason Bennett, Department of Chemistry, Penn State Erie, the Behrend College, 4701 College Drive, Erie PA 16563
Myoglobin and heme-human serum albumin (HSA) are proteins that contain iron metal centers and are thought to possess similar pathways in catalyzing nitrite reduction. However, the redox chemistry of the heme center in myoglobin is better understood than it is in HSA-heme. By comparing the catalytic effects of HSA-heme and myoglobin towards nitrite and nitric oxide reduction, the similarities and differences between the two mechanisms can be compared in order to better understand the redox behavior of HSA-heme. This presentation will focus on studying the electrochemical reduction of nitrite at HSA-heme and myoglobin. The proteins will be kept at the electrode surface by incorporating them into a film of the surfactant didodecyldimethylammonium bromide (DDAB) on glassy carbon (GC). Additionally, spectroelectrochemistry will be attempted to correlate the electrochemical changes with well-known spectroscopic observations to fully understand the nitrite reduction mechanism.
Presenter: Amanda Dynoske
Institution: Penn State- Erie, The Behrend College
Type: Poster
Subject: Chemistry
Status: Approved
